2e3a: Difference between revisions

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[[Image:2e3a.jpg|left|200px]]<br /><applet load="2e3a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2e3a.jpg|left|200px]]<br /><applet load="2e3a" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2e3a, resolution 1.30Å" />

'''Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution'''<br />

==Overview==

1.3 A resolution crystal structures of the cyanide, nitric oxide and, hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class, II peroxidase belonging to the plant peroxidase superfamily, have been, determined. Anisotropic temperature factors were introduced for all non-H, atoms of these complexes using SHELX-97 and stereochemical constraints, were applied to the protein, protoporphyrin and sugar moieties, but not to, the coordination geometries to the haem iron. These refinements identified, multiple conformations for several side chains and revised the side-chain, conformations of several residues. Little difference was observed in the, structures of the polypeptides, haem and sugar moieties and in the, coordinations to two calcium ions in these complexes. Characteristic, coordination geometries of each ligand to the haem iron were observed., CN(-) binds to the haem iron in a tilt mode (Fe...C-N = 170 degrees ), whereas NO and hydroxylamine bind in bent modes (Fe...N-O = 125 degrees, and Fe...NH(2)-OH = 111 degrees ). CN(-) is directed toward the distal, histidine (His56) and forms a hydrogen bond with the N(epsilon) atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of, ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the, plane.

1.3 A resolution crystal structures of the cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class II peroxidase belonging to the plant peroxidase superfamily, have been determined. Anisotropic temperature factors were introduced for all non-H atoms of these complexes using SHELX-97 and stereochemical constraints were applied to the protein, protoporphyrin and sugar moieties, but not to the coordination geometries to the haem iron. These refinements identified multiple conformations for several side chains and revised the side-chain conformations of several residues. Little difference was observed in the structures of the polypeptides, haem and sugar moieties and in the coordinations to two calcium ions in these complexes. Characteristic coordination geometries of each ligand to the haem iron were observed. CN(-) binds to the haem iron in a tilt mode (Fe...C-N = 170 degrees ), whereas NO and hydroxylamine bind in bent modes (Fe...N-O = 125 degrees and Fe...NH(2)-OH = 111 degrees ). CN(-) is directed toward the distal histidine (His56) and forms a hydrogen bond with the N(epsilon) atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the plane.

==About this Structure==

2E3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with MAN, CA, HEM and NO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2E3A OCA].

2E3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3A OCA].

==Reference==

Line 25:

[[Category: peroxidase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:32 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2e3a.jpg|left|200px]]<br /><applet load="2e3a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2e3a.jpg|left|200px]]<br /><applet load="2e3a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2e3a, resolution 1.30&Aring;" />
 '''Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution'''<br />
 ==Overview==
-.3 A resolution crystal structures of the cyanide, nitric oxide and, hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class, II peroxidase belonging to the plant peroxidase superfamily, have been, determined. Anisotropic temperature factors were introduced for all non-H, atoms of these complexes using SHELX-97 and stereochemical constraints, were applied to the protein, protoporphyrin and sugar moieties, but not to, the coordination geometries to the haem iron. These refinements identified, multiple conformations for several side chains and revised the side-chain, conformations of several residues. Little difference was observed in the, structures of the polypeptides, haem and sugar moieties and in the, coordinations to two calcium ions in these complexes. Characteristic, coordination geometries of each ligand to the haem iron were observed., CN(-) binds to the haem iron in a tilt mode (Fe...C-N = 170 degrees ), whereas NO and hydroxylamine bind in bent modes (Fe...N-O = 125 degrees, and Fe...NH(2)-OH = 111 degrees ). CN(-) is directed toward the distal, histidine (His56) and forms a hydrogen bond with the N(epsilon) atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of, ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the, plane.
+.3 A resolution crystal structures of the cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class II peroxidase belonging to the plant peroxidase superfamily, have been determined. Anisotropic temperature factors were introduced for all non-H atoms of these complexes using SHELX-97 and stereochemical constraints were applied to the protein, protoporphyrin and sugar moieties, but not to the coordination geometries to the haem iron. These refinements identified multiple conformations for several side chains and revised the side-chain conformations of several residues. Little difference was observed in the structures of the polypeptides, haem and sugar moieties and in the coordinations to two calcium ions in these complexes. Characteristic coordination geometries of each ligand to the haem iron were observed. CN(-) binds to the haem iron in a tilt mode (Fe...C-N = 170 degrees ), whereas NO and hydroxylamine bind in bent modes (Fe...N-O = 125 degrees and Fe...NH(2)-OH = 111 degrees ). CN(-) is directed toward the distal histidine (His56) and forms a hydrogen bond with the N(epsilon) atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the plane.
 ==About this Structure==
-E3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with MAN, CA, HEM and NO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E3A OCA].
+E3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3A OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: peroxidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:56:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:32 2008''